XA21_ORYSI
ID XA21_ORYSI Reviewed; 1025 AA.
AC Q1MX30;
DT 07-SEP-2016, integrated into UniProtKB/Swiss-Prot.
DT 30-MAY-2006, sequence version 1.
DT 03-AUG-2022, entry version 107.
DE RecName: Full=Receptor kinase-like protein Xa21 {ECO:0000303|Ref.1};
DE EC=2.7.11.1 {ECO:0000255|PROSITE-ProRule:PRU00159, ECO:0000269|PubMed:11927577};
DE Contains:
DE RecName: Full=Receptor kinase-like protein Xa21, processed {ECO:0000250|UniProtKB:Q2R2D5};
DE Flags: Precursor;
GN Name=XA21 {ECO:0000303|Ref.1};
OS Oryza sativa subsp. indica (Rice).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC Oryzoideae; Oryzeae; Oryzinae; Oryza; Oryza sativa.
OX NCBI_TaxID=39946 {ECO:0000312|EMBL:BAE93934.1};
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA Xue Q., Xu J.;
RT "Xa21 gene with bacterial blight resistance from wild rice (Oryza.
RT longistaminata) to hybrid rice(Oryza.sativa).";
RL Submitted (MAY-2006) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP FUNCTION.
RC STRAIN=cv. IRBB21;
RX PubMed=8525370; DOI=10.1126/science.270.5243.1804;
RA Song W.-Y., Wang G.-L., Chen L.-L., Kim H.-S., Pi L.-Y., Holsten T.,
RA Gardner J., Wang B., Zhai W.-X., Zhu L.-H., Fauquet C., Ronald P.;
RT "A receptor kinase-like protein encoded by the rice disease resistance
RT gene, Xa21.";
RL Science 270:1804-1806(1995).
RN [3]
RP CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, AUTOPHOSPHORYLATION,
RP COFACTOR, AND MUTAGENESIS OF LYS-736.
RX PubMed=11927577; DOI=10.1074/jbc.m110999200;
RA Liu G.-Z., Pi L.-Y., Walker J.C., Ronald P.C., Song W.-Y.;
RT "Biochemical characterization of the kinase domain of the rice disease
RT resistance receptor-like kinase XA21.";
RL J. Biol. Chem. 277:20264-20269(2002).
RN [4]
RP MUTAGENESIS OF 686-SER--SER-689 AND LYS-736, AUTOPHOSPHORYLATION, AND
RP PHOSPHORYLATION AT SER-686; THR-688 AND SER-689.
RX PubMed=16460508; DOI=10.1111/j.1365-313x.2005.02638.x;
RA Xu W.H., Wang Y.S., Liu G.Z., Chen X., Tinjuangjun P., Pi L.Y., Song W.Y.;
RT "The autophosphorylated Ser686, Thr688, and Ser689 residues in the
RT intracellular juxtamembrane domain of XA21 are implicated in stability
RT control of rice receptor-like kinase.";
RL Plant J. 45:740-751(2006).
RN [5]
RP FUNCTION, INTERACTION WITH WRKY62, AND MUTAGENESIS OF LYS-736.
RX PubMed=19825552; DOI=10.1093/mp/ssn024;
RA Peng Y., Bartley L.E., Chen X., Dardick C., Chern M., Ruan R., Canlas P.E.,
RA Ronald P.C.;
RT "OsWRKY62 is a negative regulator of basal and Xa21-mediated defense
RT against Xanthomonas oryzae pv. oryzae in rice.";
RL Mol. Plant 1:446-458(2008).
RN [6]
RP FUNCTION, PHOSPHORYLATION AT THR-705, MUTAGENESIS OF THR-680;
RP 686-SER--SER-689; SER-697; SER-699; THR-705 AND LYS-736,
RP AUTOPHOSPHORYLATION, AND INTERACTION WITH WRKY62; XB3; XB15 AND XB24.
RX PubMed=20118235; DOI=10.1074/jbc.m109.093427;
RA Chen X., Chern M., Canlas P.E., Jiang C., Ruan D., Cao P., Ronald P.C.;
RT "A conserved threonine residue in the juxtamembrane domain of the XA21
RT pattern recognition receptor is critical for kinase autophosphorylation and
RT XA21-mediated immunity.";
RL J. Biol. Chem. 285:10454-10463(2010).
CC -!- FUNCTION: [Receptor kinase-like protein Xa21]: Receptor kinase that
CC detects X.oryzae pv. oryzae protein Ax21 to promote innate immunity
CC (PubMed:20118235). Following X.oryzae pv. oryzae protein Ax21
CC detection, undergoes cleavage, releasing the processed protein kinase
CC Xa21 chain (By similarity). {ECO:0000250|UniProtKB:Q2R2D5,
CC ECO:0000269|PubMed:20118235}.
CC -!- FUNCTION: [Receptor kinase-like protein Xa21, processed]: The processed
CC protein kinase Xa21 chain released by protein cleavage after X.oryzae
CC pv. oryzae protein Ax21 detection translocates into the nucleus where
CC it can bind and regulate WRKY62, a transcription factor (By
CC similarity). Confers resistance to the bacterial pathogen X.oryzae pv.
CC oryzae (Xoo) (PubMed:8525370, PubMed:19825552, PubMed:20118235).
CC {ECO:0000250|UniProtKB:Q2R2D5, ECO:0000269|PubMed:19825552,
CC ECO:0000269|PubMed:20118235, ECO:0000269|PubMed:8525370}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-
CC [protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA-
CC COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.1;
CC Evidence={ECO:0000269|PubMed:11927577};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-threonyl-[protein] = ADP + H(+) + O-phospho-L-
CC threonyl-[protein]; Xref=Rhea:RHEA:46608, Rhea:RHEA-COMP:11060,
CC Rhea:RHEA-COMP:11605, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:61977, ChEBI:CHEBI:456216;
CC EC=2.7.11.1; Evidence={ECO:0000269|PubMed:11927577};
CC -!- COFACTOR:
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000269|PubMed:11927577};
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000269|PubMed:11927577};
CC Note=Enzymatic activity is fifteen time stronger with Mn(2+) than with
CC Mg(2+). {ECO:0000269|PubMed:11927577};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=0.3 uM for ATP {ECO:0000269|PubMed:11927577};
CC Vmax=8.4 nmol/min/mg enzyme with ATP as substrate
CC {ECO:0000269|PubMed:11927577};
CC -!- SUBUNIT: Binds to XB3, XB15 and XB24 (PubMed:20118235). Receptor
CC kinase-like protein Xa21, processed: Interacts with WRKY62/XB10 in the
CC nucleus (PubMed:19825552, PubMed:20118235).
CC {ECO:0000269|PubMed:19825552, ECO:0000269|PubMed:20118235}.
CC -!- SUBCELLULAR LOCATION: [Receptor kinase-like protein Xa21]: Cell
CC membrane {ECO:0000250|UniProtKB:Q2R2D5}; Single-pass membrane protein
CC {ECO:0000255}. Endoplasmic reticulum membrane
CC {ECO:0000250|UniProtKB:Q2R2D5}; Single-pass membrane protein
CC {ECO:0000255}. Note=Present in cortical and perinuclear endoplasmic
CC reticulum. Cleaved upon X.oryzae pv. oryzae protein Ax21 recognition;
CC the kinase containing fragment is translocated into the nucleus.
CC {ECO:0000250|UniProtKB:Q2R2D5}.
CC -!- SUBCELLULAR LOCATION: [Receptor kinase-like protein Xa21, processed]:
CC Nucleus {ECO:0000250|UniProtKB:Q2R2D5}.
CC -!- PTM: Undergoes protein cleavage upon X.oryzae pv. oryzae protein Ax21
CC detection, thus releasing the processed protein kinase Xa21 chain.
CC {ECO:0000250|UniProtKB:Q2R2D5}.
CC -!- PTM: Autophosphorylated on serine and threonine residues; these
CC phosphorylation prevents proteolytic degradation.
CC {ECO:0000269|PubMed:11927577, ECO:0000269|PubMed:16460508,
CC ECO:0000269|PubMed:20118235}.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. Ser/Thr protein
CC kinase family. {ECO:0000255|PROSITE-ProRule:PRU00159}.
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DR EMBL; AB212798; BAE93933.1; -; Genomic_DNA.
DR EMBL; AB212799; BAE93934.1; -; Genomic_DNA.
DR AlphaFoldDB; Q1MX30; -.
DR SMR; Q1MX30; -.
DR iPTMnet; Q1MX30; -.
DR PRIDE; Q1MX30; -.
DR SABIO-RK; Q1MX30; -.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0106310; F:protein serine kinase activity; IEA:RHEA.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; IDA:UniProtKB.
DR GO; GO:0006952; P:defense response; IEA:UniProtKB-KW.
DR GO; GO:0031349; P:positive regulation of defense response; IMP:UniProtKB.
DR GO; GO:1900426; P:positive regulation of defense response to bacterium; IDA:UniProtKB.
DR GO; GO:0046777; P:protein autophosphorylation; IDA:UniProtKB.
DR Gene3D; 3.80.10.10; -; 3.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR001611; Leu-rich_rpt.
DR InterPro; IPR003591; Leu-rich_rpt_typical-subtyp.
DR InterPro; IPR032675; LRR_dom_sf.
DR InterPro; IPR013210; LRR_N_plant-typ.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR017441; Protein_kinase_ATP_BS.
DR InterPro; IPR008271; Ser/Thr_kinase_AS.
DR Pfam; PF00560; LRR_1; 1.
DR Pfam; PF13855; LRR_8; 3.
DR Pfam; PF08263; LRRNT_2; 1.
DR Pfam; PF00069; Pkinase; 1.
DR SMART; SM00369; LRR_TYP; 12.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF56112; SSF56112; 1.
DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PE 1: Evidence at protein level;
KW ATP-binding; Cell membrane; Endoplasmic reticulum; Glycoprotein; Kinase;
KW Leucine-rich repeat; Membrane; Nucleotide-binding; Nucleus; Phosphoprotein;
KW Plant defense; Receptor; Repeat; Serine/threonine-protein kinase; Signal;
KW Transferase; Transmembrane; Transmembrane helix.
FT SIGNAL 1..23
FT /evidence="ECO:0000255"
FT CHAIN 24..1025
FT /note="Receptor kinase-like protein Xa21"
FT /id="PRO_5005930761"
FT CHAIN ?..1025
FT /note="Receptor kinase-like protein Xa21, processed"
FT /id="PRO_0000436963"
FT TOPO_DOM 24..653
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 654..674
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 675..1025
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT REPEAT 78..101
FT /note="LRR 1"
FT /evidence="ECO:0000255"
FT REPEAT 102..126
FT /note="LRR 2"
FT /evidence="ECO:0000255"
FT REPEAT 127..150
FT /note="LRR 3"
FT /evidence="ECO:0000255"
FT REPEAT 152..174
FT /note="LRR 4"
FT /evidence="ECO:0000255"
FT REPEAT 176..199
FT /note="LRR 5"
FT /evidence="ECO:0000255"
FT REPEAT 200..223
FT /note="LRR 6"
FT /evidence="ECO:0000255"
FT REPEAT 224..247
FT /note="LRR 7"
FT /evidence="ECO:0000255"
FT REPEAT 248..271
FT /note="LRR 8"
FT /evidence="ECO:0000255"
FT REPEAT 273..296
FT /note="LRR 9"
FT /evidence="ECO:0000255"
FT REPEAT 298..319
FT /note="LRR 10"
FT /evidence="ECO:0000255"
FT REPEAT 320..343
FT /note="LRR 11"
FT /evidence="ECO:0000255"
FT REPEAT 350..373
FT /note="LRR 12"
FT /evidence="ECO:0000255"
FT REPEAT 375..399
FT /note="LRR 13"
FT /evidence="ECO:0000255"
FT REPEAT 400..423
FT /note="LRR 14"
FT /evidence="ECO:0000255"
FT REPEAT 425..447
FT /note="LRR 15"
FT /evidence="ECO:0000255"
FT REPEAT 448..470
FT /note="LRR 16"
FT /evidence="ECO:0000255"
FT REPEAT 471..495
FT /note="LRR 17"
FT /evidence="ECO:0000255"
FT REPEAT 497..520
FT /note="LRR 18"
FT /evidence="ECO:0000255"
FT REPEAT 521..544
FT /note="LRR 19"
FT /evidence="ECO:0000255"
FT REPEAT 545..568
FT /note="LRR 20"
FT /evidence="ECO:0000255"
FT REPEAT 569..592
FT /note="LRR 21"
FT /evidence="ECO:0000255"
FT REPEAT 594..617
FT /note="LRR 22"
FT /evidence="ECO:0000255"
FT DOMAIN 708..979
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT ACT_SITE 842
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 714..722
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 736
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT MOD_RES 686
FT /note="Phosphoserine; by autocatalysis"
FT /evidence="ECO:0000269|PubMed:16460508"
FT MOD_RES 688
FT /note="Phosphothreonine; by autocatalysis"
FT /evidence="ECO:0000269|PubMed:16460508"
FT MOD_RES 689
FT /note="Phosphoserine; by autocatalysis"
FT /evidence="ECO:0000269|PubMed:16460508"
FT MOD_RES 705
FT /note="Phosphothreonine; by autocatalysis"
FT /evidence="ECO:0000269|PubMed:20118235"
FT CARBOHYD 55
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 90
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 101
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 198
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 235
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 246
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 295
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 322
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 349
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 373
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 435
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 446
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 470
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 483
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 503
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 580
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 599
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT MUTAGEN 680
FT /note="T->A: Increased autophosphorylation."
FT /evidence="ECO:0000269|PubMed:20118235"
FT MUTAGEN 686..689
FT /note="SRTS->ARAA: Normal autophosphorylation but reduced
FT stability leading to increased proteolytic cleavage and
FT compromised resistance to X.oryzae pv. oryzae (Xoo)."
FT /evidence="ECO:0000269|PubMed:16460508,
FT ECO:0000269|PubMed:20118235"
FT MUTAGEN 697
FT /note="S->A,D: Slight reduction in autophosphorylation."
FT /evidence="ECO:0000269|PubMed:20118235"
FT MUTAGEN 699
FT /note="S->A: Increased autophosphorylation."
FT /evidence="ECO:0000269|PubMed:20118235"
FT MUTAGEN 705
FT /note="T->A,E: Abolished autophosphorylation and loss of
FT interactions with target proteins (e.g. WRKY62/XB10, XB3,
FT XB15 and XB24). Loss of positive impact on innate immunity
FT toward X.oryzae pv. oryzae (Xoo)."
FT /evidence="ECO:0000269|PubMed:20118235"
FT MUTAGEN 736
FT /note="K->E: Kinase-deficient mutant lacking
FT autophosphorylation, impaired interaction with WRKY62.
FT Reduced stability leading to increased proteolytic
FT cleavage."
FT /evidence="ECO:0000269|PubMed:11927577,
FT ECO:0000269|PubMed:16460508, ECO:0000269|PubMed:19825552,
FT ECO:0000269|PubMed:20118235"
SQ SEQUENCE 1025 AA; 111339 MW; B55D4FD938229D9B CRC64;
MISLPLLLFV LLFSALLLCP SSSDDDGDAA GDELALLSFK SSLLYQGGQS LASWNTSGHG
QHCTWVGVVC GRRRRRHPHR VVKLLLRSSN LSGIISPSLG NLSFLRELDL GDNYLSGEIP
PELSRLSRLQ LLELSDNSIQ GSIPAAIGAC TKLTSLDLSH NQLRGMIPRE IGASLKHLSN
LYLYKNGLSG EIPSALGNLT SLQEFDLSFN RLSGAIPSSL GQLSSLLTMN LGQNNLSGMI
PNSIWNLSSL RAFSVRENKL GGMIPTNAFK TLHLLEVIDM GTNRFHGKIP ASVANASHLT
VIQIYGNLFS GIITSGFGRL RNLTELYLWR NLFQTREQDD WGFISDLTNC SKLQTLNLGE
NNLGGVLPNS FSNLSTSLSF LALELNKITG SIPKDIGNLI GLQHLYLCNN NFRGSLPSSL
GRLKNLGILL AYENNLSGSI PLAIGNLTEL NILLLGTNKF SGWIPYTLSN LTNLLSLGLS
TNNLSGPIPS ELFNIQTLSI MINVSKNNLE GSIPQEIGHL KNLVEFHAES NRLSGKIPNT
LGDCQLLRYL YLQNNLLSGS IPSALGQLKG LETLDLSSNN LSGQIPTSLA DITMLHSLNL
SFNSFVGEVP TIGAFAAASG ISIQGNAKLC GGIPDLHLPR CCPLLENRKH FPVLPISVSL
AAALAILSSL YLLITWHKRT KKGAPSRTSM KGHPLVSYSQ LVKATDGFAP TNLLGSGSFG
SVYKGKLNIQ DHVAVKVLKL ENPKALKSFT AECEALRNMR HRNLVKIVTI CSSIDNRGND
FKAIVYDFMP NGSLEDWIHP ETNDQADQRH LNLHRRVTIL LDVACALDYL HRHGPEPVVH
CDIKSSNVLL DSDMVAHVGD FGLARILVDG TSLIQQSTSS MGFIGTIGYA APEYGVGLIA
STHGDIYSYG ILVLEIVTGK RPTDSTFRPD LGLRQYVELG LHGRVTDVVD TKLILDSENW
LNSTNNSPCR RITECIVWLL RLGLSCSQEL PSSRTPTGDI IDELNAIKQN LSGLFPVCEG
GSLEF
